Sirtuins are enzymes that play critical roles in many cellular epigenetic or metabolic pathways. In mammalian cells, seven sirtuin homologs have been identified, referred to as SIRTUINS 1-7 or SIRT1-7. SIRT6 is localized in the cell nucleus (of human keratinocytes and dermal fibroblasts, for example) and is a member of the conserved family of sirtuin proteins which are associated with metabolism and longevity. SIRT6 is a histone 3, lysine 9 (H3K9) deacetylase, and is primarily involved in DNA repair and telomere stability.
The term “SIRT6 activating peptide” means a peptide that causes the amount of SIRT6 in the cell to increase by whatever pathway causes that result. US2011-0318284, which is hereby incorporated by reference in its entirety, discloses compositions comprising SIRT6 activating peptides. The peptides are derived from highly conserved regions of human SIRT proteins. Of the eight peptide sequences disclosed in US2011-0318284, the following sequence is of interest here:
(SEQ ID No. 1)G-A-G-V-S-A-E-NH2Gly-Ala-Gly-Val-Ser-Ala-Glu-NH2
Note that the NH2 group on the C-terminal end of the peptide has been substituted onto the peptide to improve the resistance of the peptide to certain forms of degradation. NH2 in that position does not occur naturally.
This peptide was reported to increase sirtuin 6 expression very significantly in normal human fibroblasts and normal human keratinocytes in short-term cultures. In addition, the sirtuin 6 expression stimulation effect was maintained for the long term. According to the reference, the activating peptides may be used alone or in combination with at least one other active agent, in a physiologically acceptable medium. The reference also discloses the utilization of a cosmetic composition to prevent and/or repair DNA degradation, improve telomere maintenance and reduce cellular senescence. However, US2011-0318284 makes no mention of Arabidopsis thaliana. 
Co-pending application U.S. Ser. No. 14/045,075, filed Oct. 3, 2013 discloses compositions comprising the same SIRT6 activating peptides as US2011-0318284. According to this reference, a SIRT6 activating peptide may be present in the composition in amounts ranging from 0.0001 to 8%, preferably from about 0.001 to 3%, more preferably from about 0.01 to 1%. In a preferred embodiment, the activating peptide is supplied as a component of a yeast extract.
U.S. Ser. No. 14/045,075 also reports that a dose dependent increase in SIRT6 expression in Normal Human Epidermal Keratinocytes (NHEK) was caused by the SIRT6 activating peptide:
(SEQ ID No. 1) G-A-G-V-S-A-E-NH2Gly-Ala-Gly-Val-Ser-Ala-Glu-NH2
It has been further reported that an unexpected increase in collagen synthesis in normal human dermal fibroblasts is caused by a combination of Laminaria digitata extract, Narcissus tazetta bulb extract, and a yeast protein extract that contains this SIRT6 activating peptide (SEQ ID 1). Furthermore, U.S. Ser. No. 14/045,075 mentions Arabidopsis thaliana extract in a long list of optional botanical extracts, wherein the suggested ranges for the one or more optional botanical extracts are reported as about 0.0001 to 10%, preferably about 0.0005 to 8%, more preferably about 0.001 to 5% by weight of the total composition. However, the Arabidopsis thaliana extract is not noted for any particular activity, and no synergy is disclosed between Arabidopsis thaliana extract and any of the SIRT6 activating peptides disclosed therein.
Arabidopsis thaliana Extract Containing 8-Oxoguanine Glycosylase
8-Oxoguanine glycosylase (OGG1) is a DNA repair enzyme that excises 8-oxoguanine, a base byproduct resulting from exposure to reactive oxygen species and ionizing radiation. OGG1 is active in both genomic and mitochondrial DNA, including in skin cells. 8-Oxoguanine glycosylase can be obtained by yeast fermentation of the plant Arabidopsis thaliana. Arabidopsis thaliana is a species in the Brassicaceae family, and is well known, as it is one of the model organisms used for studying plant biology. 8-Oxoguanine glycosylase extract from Arabidopsis thaliana ferment is commercially available in a liposomal formulation containing lecithin and water under the tradename Roxisomes™, from Barnet Products Corp., Englewood Cliffs, N.J. About 0.5% of the Roxisome™ is 8-Oxoguanine glycosylase.
Revoris is a commercially available wrinkle treatment product that reportedly comprises Roxisomes™ and two peptides: palmitoyl oligopeptide (a three amino acid peptide) and palmitoyl tetrapeptide-7 (a four amino acid peptide). Neither of these peptides is the same as nor suggests the 7 amino acid peptide SEQ. ID 1. No synergy is suggested between the Roxisomes and the peptides of Revoris.